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1B6L

HIV-1 PROTEASE COMPLEXED WITH MACROCYCLIC PEPTIDOMIMETIC INHIBITOR 4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
AGLY68
AHIS69
ALYS70
BPRO101
BLYS155

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH396
APRO1
AARG57
AHIS69
AHOH325

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG14
AGLY17
AHOH379
AHOH394
BGLY116
BGLY117
BHOH311
BHOH317

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PI4 A 201
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH301
AHOH320
AHOH321
BASP125
BGLY127
BGLY148
BGLY149
BVAL182
BILE184

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AGLY78
BGLY178

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AGLY78
BGLY178

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

221716

PDB entries from 2024-06-26

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